CHELATION OF MERCURY BY OUABAIN-SENSITIVE AND OUABAIN-RESISTANT RENAL NA,K-ATPASE

被引：18
|
作者：
ANNER, BM
MOOSMAYER, M
IMESCH, E
机构：
[1] Department of Pharmacology, Geneva University Medical Center
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 167卷 / 03期
关键词：
D O I：
10.1016/0006-291X(90)90638-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The SH-reactive HgCl2 inhibits the Na,K-ATPase activity potently in a manner antagonized only partially by EDTA or cysteine; solely dimercaprol, a dithiol antidote for mercury, blocks the HgCl2 effects entirely as confirmed also by 203Hg-binding experiments. The results reveal the presence of a chelating component in pure Na,K-ATPase with an affinity for mercury superior to EDTA. The mercury-sensitivity of the Na,K-ATPase is not related to the ouabain-sensitivity. This criterion will be useful for the distinction between ouabain-like and mercury-like inhibitors from body fluids and tissues. © 1990.
引用
收藏
页码：1115 / 1121
页数：7
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